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Vol. 273, Issue 3, 1583-1590, January 16, 1998
From the Department of Molecular Physiology, National
Cardiovascular Center Research Institute, Fujishiro-dai 5-7, Suita,
Osaka 565, Japan
The rat L6 skeletal muscle cell line was used to
study expression of the dystrophin-containing glycoprotein complex and
its interaction with the integrin system involved in the cell-matrix adhesion reaction. A complex of dystrophin and its associated proteins
was fully expressed in L6 myotubes, from which anti-dystrophin or
anti-
Bidirectional Signaling between Sarcoglycans and the Integrin
Adhesion System in Cultured L6 Myocytes
-sarcoglycan co-precipitated integrin
5
1 and other focal
adhesion-associated proteins vinculin, talin, paxillin, and focal
adhesion kinase. Immunostaining and confocal microscopy revealed that
dystrophin, -sarcoglycan, integrin 51,
and vinculin exhibited overlapping distribution in the sarcolemma,
especially at focal adhesion-like, spotty structures. Adhesion of cells
to fibronectin- or collagen type I-coated dishes resulted in induction of tyrosine phosphorylation of - and 
-sarcoglycans but not
-sarcoglycan. The same proteins were also tyrosine-phosphorylated
when L6 cells in suspension were exposed to Arg-Gly-Asp-Ser peptide.
All of these tyrosine phosphorylations were inhibited by herbimycin A. On the other hand, treatment of L6 myotubes with - and
-sarcoglycan antisense oligodeoxynucleotides resulted in complete
disappearance of - and -sarcoglycans and in significant reduction
of levels of the associated focal adhesion proteins, which caused about 50% reduction of cell adhesion. These results indicate the existence of bidirectional communication between the dystrophin-containing complex and the integrin adhesion system in cultured L6 myocytes.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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